Journal article Open Access
Research data supporting: "Understanding functional group and assembly dynamics in temperature responsive systems leads to design principles for enzyme responsive assemblies"
Liu, Hongxu;
Lionello, Chiara;
Westley, Jenna;
Cardellini, Annalisa;
Huynh, Uyen;
Pavan, Giovanni Maria;
Thayumanavan, S.
This repository contains the set of data shown in the paper "Understanding functional group and assembly dynamics in temperature responsive systems leads to design principles for enzyme responsive assemblies", published on Nanoscale (DOI: 10.1039/D1NR02000E).
Understanding the molecular rules behind the dynamics of supramolecular assemblies is fundamentally important for the rational design of responsive assemblies with tunable properties. Herein, we report that the dynamics of temperature-sensitive supramolecular assemblies is not only affected by the dehydration of oligoethylene glycol (OEG) motifs, but also by the thermally-promoted molecular motions. These counteracting features set up a dynamics transition point (DTP) that can be modulated with subtle variations in a small hydrophobic patch on the hydrophilic face of the amphiphilic assembly. Understanding the structural factors that control the dynamics of the assemblies leads to rational design of enzyme-responsive assemblies with tunable temperature responsive profiles.
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TSensitiveSupramolecularAssembly.zip
md5:4252b55a92476658ad1025a486e0f20e |
1.2 MB | Download |
| All versions | This version | |
|---|---|---|
| Views | 18 | 18 |
| Downloads | 1 | 1 |
| Data volume | 1.2 MB | 1.2 MB |
| Unique views | 15 | 15 |
| Unique downloads | 1 | 1 |
- Publication date:
- June 18, 2021
- DOI:
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- Grants:
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European Commission:
- DYNAPOL - Modeling approaches toward bioinspired dynamic materials (818776)
- Multiscale Modeling of Self-Assembled Polymeric Nanocarriers Responding to Specific Protein Stimuli (200021_175735)
- Communities:
- License (for files):
- Creative Commons Attribution 4.0 International